SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O15169

- AXIN1_HUMAN

UniProt

O15169 - AXIN1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Axin-1
Gene
AXIN1, AXIN
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7. Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development.3 Publications

GO - Molecular functioni

  1. GTPase activator activity Source: RefGenome
  2. I-SMAD binding Source: BHF-UCL
  3. SMAD binding Source: BHF-UCL
  4. armadillo repeat domain binding Source: BHF-UCL
  5. beta-catenin binding Source: BHF-UCL
  6. enzyme binding Source: UniProtKB
  7. identical protein binding Source: BHF-UCL
  8. protein binding Source: UniProtKB
  9. protein complex scaffold Source: BHF-UCL
  10. protein homodimerization activity Source: UniProtKB
  11. protein kinase binding Source: BHF-UCL
  12. signal transducer activity Source: BHF-UCL
  13. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. Wnt signaling pathway involved in somitogenesis Source: RefGenome
  2. Wnt-activated signaling pathway involved in forebrain neuron fate commitment Source: RefGenome
  3. activation of JUN kinase activity Source: RefGenome
  4. activation of protein kinase activity Source: BHF-UCL
  5. apoptotic process Source: UniProtKB-KW
  6. axial mesoderm formation Source: RefGenome
  7. canonical Wnt signaling pathway Source: UniProtKB
  8. canonical Wnt signaling pathway involved in neural plate anterior/posterior pattern formation Source: RefGenome
  9. cell death Source: RefGenome
  10. cellular protein complex assembly Source: BHF-UCL
  11. cellular response to organic cyclic compound Source: RefGenome
  12. cytoplasmic microtubule organization Source: RefGenome
  13. determination of left/right symmetry Source: RefGenome
  14. dorsal/ventral axis specification Source: RefGenome
  15. embryonic eye morphogenesis Source: RefGenome
  16. embryonic skeletal joint morphogenesis Source: RefGenome
  17. forebrain anterior/posterior pattern specification Source: RefGenome
  18. genetic imprinting Source: Ensembl
  19. in utero embryonic development Source: Ensembl
  20. muscle cell development Source: RefGenome
  21. negative regulation of Wnt signaling pathway Source: BHF-UCL
  22. negative regulation of canonical Wnt signaling pathway Source: RefGenome
  23. negative regulation of fat cell differentiation Source: RefGenome
  24. negative regulation of protein metabolic process Source: Ensembl
  25. negative regulation of transcription elongation from RNA polymerase II promoter Source: Ensembl
  26. nucleocytoplasmic transport Source: Ensembl
  27. olfactory placode formation Source: RefGenome
  28. optic placode formation Source: RefGenome
  29. positive regulation of GTPase activity Source: GOC
  30. positive regulation of JNK cascade Source: UniProtKB
  31. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  32. positive regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
  33. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  34. positive regulation of protein catabolic process Source: BHF-UCL
  35. positive regulation of protein phosphorylation Source: BHF-UCL
  36. positive regulation of protein ubiquitination Source: BHF-UCL
  37. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
  38. positive regulation of transcription, DNA-templated Source: BHF-UCL
  39. positive regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  40. positive regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  41. post-anal tail morphogenesis Source: Ensembl
  42. protein catabolic process Source: Ensembl
  43. protein homooligomerization Source: Ensembl
  44. protein polyubiquitination Source: Ensembl
  45. regulation of catenin import into nucleus Source: RefGenome
  46. sensory perception of sound Source: Ensembl
  47. termination of G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Apoptosis, Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_200766. degradation of AXIN.
REACT_200777. TCF dependent signaling in response to WNT.
SignaLinkiO15169.

Names & Taxonomyi

Protein namesi
Recommended name:
Axin-1
Alternative name(s):
Axis inhibition protein 1
Short name:
hAxin
Gene namesi
Name:AXIN1
Synonyms:AXIN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:903. AXIN1.

Subcellular locationi

Cytoplasm. Nucleus. Membrane By similarity. Cell membrane By similarity
Note: MACF1 is required for its translocation to cell membrane By similarity. On UV irradiation, translocates to the nucleus and colocalizes with DAAX.3 Publications

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. beta-catenin destruction complex Source: UniProtKB
  3. cell cortex Source: RefGenome
  4. cell periphery Source: BHF-UCL
  5. cytoplasm Source: UniProtKB
  6. cytoplasmic membrane-bounded vesicle Source: RefGenome
  7. cytoplasmic microtubule Source: RefGenome
  8. cytoplasmic vesicle Source: BHF-UCL
  9. cytosol Source: Reactome
  10. lateral plasma membrane Source: MGI
  11. nucleus Source: UniProtKB
  12. perinuclear region of cytoplasm Source: BHF-UCL
  13. postsynaptic density Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes.
Note: The gene represented in this entry is involved in disease pathogenesis.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061L → R in HCC. 1 Publication
VAR_015589
Natural varianti345 – 3451P → L in HCC. 1 Publication
VAR_015590
Natural varianti425 – 4251G → S in HCC. 1 Publication
Corresponds to variant rs116350678 [ dbSNP | Ensembl ].
VAR_015591
Natural varianti650 – 6501G → S in HCC and in hepatoblastoma. 1 Publication
Corresponds to variant rs117208012 [ dbSNP | Ensembl ].
VAR_015592
Caudal duplication anomaly (CADUA) [MIM:607864]: A condition characterized by the occurrence of duplications of different organs in the caudal region.
Note: The disease is caused by mutations affecting the gene represented in this entry. Caudal duplication anomaly is associated with hypermethylation of the AXIN1 promoter.1 Publication

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

MIMi114550. phenotype.
607864. phenotype.
PharmGKBiPA25195.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 862862Axin-1
PRO_0000220888Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei75 – 751Phosphoserine; by CK11 Publication
Modified residuei77 – 771Phosphoserine; by CK11 Publication
Modified residuei217 – 2171Phosphoserine; by CK11 Publication
Modified residuei469 – 4691Phosphoserine; by CK11 Publication
Modified residuei481 – 4811Phosphothreonine; by GSK3-beta Inferred
Modified residuei486 – 4861Phosphoserine; by GSK3-beta By similarity
Modified residuei493 – 4931Phosphoserine By similarity
Cross-linki857 – 857Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-linki860 – 860Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Post-translational modificationi

Phosphorylation and dephosphorylation of AXIN1 regulates assembly and function of the beta-catenin complex. Phosphorylated by CK1 and GSK3B. Dephosphorylated by PPP1CA and PPP2CA. Phosphorylation by CK1 enhances binding of GSK3B to AXIN1.2 Publications
ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination at 'Lys-48' and subsequent activation of the Wnt signaling pathway.
Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Sumoylation at Lys-857 and Lys-860 prevents ubiquitination and degradation. Sumoylation is required for AXIN1-mediated JNK activation. Deubiquitinated by USP34, deubiquitinated downstream of beta-catenin stabilization step: deubiquitination is important for nuclear accumulation during Wnt signaling to positively regulate beta-catenin (CTNBB1)-mediated transcription.4 Publications

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO15169.
PaxDbiO15169.
PRIDEiO15169.

PTM databases

PhosphoSiteiO15169.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

ArrayExpressiO15169.
BgeeiO15169.
CleanExiHS_AXIN1.
GenevestigatoriO15169.

Organism-specific databases

HPAiCAB012987.

Interactioni

Subunit structurei

Homodimer. Interacts with ZBED3; the interaction is direct, enhanced by protein kinase GSK3B and casein kinase CSNK1E activities and decreases GSK3B-induced beta-catenin serine and threonine phosphorylations By similarity. Component of the beta-catenin destruction complex, containing at least, CTNNB1, an axin and GSK3B, that regulates CTNNB1 protein levels through phosphorylation and ubiquitination. Interacts with CTNNB1 (via the armadillo repeats 2-7). Interacts with GSK3B; the interaction hyperphosphorylates CTNNB1 leading to its ubiquitination and destruction. Component of the AXIN1-HIPK2-TP53 complex. Interacts directly in the complex with TP53 and HIPK2. Interacts with DAXX; the interaction stimulates the interaction of DAXX with TP53, stimulates 'Ser-46' phosphorylation of TP53 and induces cell death on UV irradiation. Also binds APC, SMAD6, SMAD7 and RNF111. Interacts with DIXDC1; prevents interaction with MAP3K1. Interacts with MAP3K4. Interacts with ANKRD6 and AIDA By similarity. Interacts with MDFI; the interaction decreases AXIN1-mediated JUN N-terminal kinase (JNK) activation. Interacts with MDFIC; the interaction inhibits beta-cateninin-mediated signaling and AXIN1-mediated JUN N-terminal kinase (JNK) activation. Interacts with LRP5 (via its phosphorylated PPPSP motifs); the interaction is stimulated by WNT1 and GSK3B and activates beta-catenin signaling. Interacts (via the C-terminal) with PPP1CA; the interaction dephosphorylates AXIN1 and regulates interaction with GSK3B. Interacts with PPP2CA; the interaction dephosphorylates AXIN1. Interacts with MACF1 By similarity. Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B By similarity. Interacts with TNKS. Interacts with DAB2; the interaction is mutually exclusive with the AXIN1:PPP1CA interaction.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANP32AP396872EBI-710484,EBI-359234
apcP700392EBI-710484,EBI-8069633From a different organism.
CRMP1Q141942EBI-710484,EBI-473101
CSNK1EP496744EBI-710484,EBI-749343
CTNNB1P3522226EBI-710484,EBI-491549
Ctnnb1Q022485EBI-710484,EBI-397872From a different organism.
FBXW11Q9UKB14EBI-710484,EBI-355189
GSK3AP498402EBI-710484,EBI-1044067
GSK3BP4984131EBI-710484,EBI-373586
MYCP0110610EBI-710484,EBI-447544
PPM1AP358132EBI-710484,EBI-989143
PPP1CAP621364EBI-710484,EBI-357253
RNF111Q6ZNA42EBI-710484,EBI-2129175
Rnf111Q99ML95EBI-710484,EBI-646015From a different organism.
SMAD7O151058EBI-710484,EBI-3861591
TNKS2Q9H2K22EBI-710484,EBI-4398527
TP53P046374EBI-710484,EBI-366083
TRIM29Q141342EBI-710484,EBI-702370
TUBG1P232584EBI-710484,EBI-302589

Protein-protein interaction databases

BioGridi113909. 55 interactions.
DIPiDIP-34630N.
IntActiO15169. 62 interactions.
MINTiMINT-100969.
STRINGi9606.ENSP00000262320.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi81 – 877
Helixi89 – 924
Helixi96 – 10712
Turni108 – 1103
Helixi112 – 12615
Helixi131 – 1333
Helixi134 – 14815
Helixi155 – 1595
Helixi162 – 17413
Turni179 – 1824
Helixi183 – 19513
Helixi197 – 2015
Helixi205 – 2084
Turni209 – 2124
Helixi385 – 40016

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DK8X-ray1.57A74-220[»]
1EMUX-ray1.90A80-211[»]
1O9UX-ray2.40B383-400[»]
3ZDIX-ray2.64B383-400[»]
4B7TX-ray2.77B383-400[»]
4NM0X-ray2.50B383-402[»]
4NM3X-ray2.10B383-402[»]
4NM5X-ray2.30B383-402[»]
4NM7X-ray2.30B383-402[»]
4NU1X-ray2.50B383-402[»]
ProteinModelPortaliO15169.
SMRiO15169. Positions 74-220, 779-862.

Miscellaneous databases

EvolutionaryTraceiO15169.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 211124RGS
Add
BLAST
Domaini780 – 86283DIX
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni209 – 338130Interaction with TP53 By similarity
Add
BLAST
Regioni348 – 43386Interaction with GSK3B By similarity
Add
BLAST
Regioni434 – 50269Interaction with CTNNB1 By similarity
Add
BLAST
Regioni507 – 757251Interaction with RNF111
Add
BLAST
Regioni575 – 789215Interaction with PPP2CA
Add
BLAST
Regioni677 – 75276Interaction with HIPK2 By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi20 – 2910Tankyrase-binding motif

Domaini

The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2.1 Publication

Sequence similaritiesi

Contains 1 DIX domain.
Contains 1 RGS domain.

Phylogenomic databases

eggNOGiNOG238205.
HOVERGENiHBG004324.
InParanoidiO15169.
KOiK02157.
OMAiIMQWIIE.
OrthoDBiEOG79PJQ0.
PhylomeDBiO15169.
TreeFamiTF315454.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR014936. Axin_b-cat-bd.
IPR001158. DIX.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF08833. Axin_b-cat_bind. 1 hit.
PF00778. DIX. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00021. DAX. 1 hit.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50841. DIX. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15169-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MNIQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDPRPA SYSFCSGKGV    50
GIKGETSTAT PRRSDLDLGY EPEGSASPTP PYLKWAESLH SLLDDQDGIS 100
LFRTFLKQEG CADLLDFWFA CTGFRKLEPC DSNEEKRLKL ARAIYRKYIL 150
DNNGIVSRQT KPATKSFIKG CIMKQLIDPA MFDQAQTEIQ ATMEENTYPS 200
FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGISGYLPT LNEDEEWKCD 250
QDMDEDDGRD AAPPGRLPQK LLLETAAPRV SSSRRYSEGR EFRYGSWREP 300
VNPYYVNAGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK 350
QHRREMQESV QVNGRVPLPH IPRTYRVPKE VRVEPQKFAE ELIHRLEAVQ 400
RTREAEEKLE ERLKRVRMEE EGEDGDPSSG PPGPCHKLPP APAWHHFPPR 450
CVDMGCAGLR DAHEENPESI LDEHVQRVLR TPGRQSPGPG HRSPDSGHVA 500
KMPVALGGAA SGHGKHVPKS GAKLDAAGLH HHRHVHHHVH HSTARPKEQV 550
EAEATRRAQS SFAWGLEPHS HGARSRGYSE SVGAAPNASD GLAHSGKVGV 600
ACKRNAKKAE SGKSASTEVP GASEDAEKNQ KIMQWIIEGE KEISRHRRTG 650
HGSSGTRKPQ PHENSRPLSL EHPWAGPQLR TSVQPSHLFI QDPTMPPHPA 700
PNPLTQLEEA RRRLEEEEKR ASRAPSKQRY VQEVMRRGRA CVRPACAPVL 750
HVVPAVSDME LSETETRSQR KVGGGSAQPC DSIVVAYYFC GEPIPYRTLV 800
RGRAVTLGQF KELLTKKGSY RYYFKKVSDE FDCGVVFEEV REDEAVLPVF 850
EEKIIGKVEK VD 862
Length:862
Mass (Da):95,635
Last modified:May 10, 2002 - v2
Checksum:i10779173F5092F3F
GO
Isoform 2 (identifier: O15169-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     730-765: Missing.

Show »
Length:826
Mass (Da):91,653
Checksum:i4AA4187D70A5863D
GO

Sequence cautioni

The sequence AAC51624.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061L → R in HCC. 1 Publication
VAR_015589
Natural varianti345 – 3451P → L in HCC. 1 Publication
VAR_015590
Natural varianti425 – 4251G → S in HCC. 1 Publication
Corresponds to variant rs116350678 [ dbSNP | Ensembl ].
VAR_015591
Natural varianti650 – 6501G → S in HCC and in hepatoblastoma. 1 Publication
Corresponds to variant rs117208012 [ dbSNP | Ensembl ].
VAR_015592
Natural varianti841 – 8411R → Q in hepatoblastoma. 1 Publication
Corresponds to variant rs34015754 [ dbSNP | Ensembl ].
VAR_015593

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei730 – 76536Missing in isoform 2.
VSP_019398Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti360 – 3601V → A in AAC51624. 1 Publication
Sequence conflicti451 – 4555CVDMG → LCWTWA in AAC51624. 1 Publication
Sequence conflicti482 – 4821P → T in AAC51624. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF009674 mRNA. Translation: AAC51624.1. Different initiation.
AE006463 Genomic DNA. Translation: AAK61224.1.
Z69667, AC005202, Z99754 Genomic DNA. Translation: CAI95589.2.
Z69667, AC005202, Z99754 Genomic DNA. Translation: CAI95590.2.
Z99754, AC005202, Z69667 Genomic DNA. Translation: CAI95600.2.
Z99754, AC005202, Z69667 Genomic DNA. Translation: CAI95601.2.
BC017447 mRNA. Translation: AAH17447.1.
BC044648 mRNA. Translation: AAH44648.1.
CCDSiCCDS10405.1. [O15169-1]
CCDS10406.1. [O15169-2]
RefSeqiNP_003493.1. NM_003502.3. [O15169-1]
NP_851393.1. NM_181050.2. [O15169-2]
XP_005255666.1. XM_005255609.2. [O15169-1]
UniGeneiHs.592082.

Genome annotation databases

EnsembliENST00000262320; ENSP00000262320; ENSG00000103126. [O15169-1]
ENST00000354866; ENSP00000346935; ENSG00000103126. [O15169-2]
GeneIDi8312.
KEGGihsa:8312.
UCSCiuc002cgp.2. human. [O15169-1]
uc002cgq.2. human. [O15169-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF009674 mRNA. Translation: AAC51624.1 . Different initiation.
AE006463 Genomic DNA. Translation: AAK61224.1 .
Z69667 , AC005202 , Z99754 Genomic DNA. Translation: CAI95589.2 .
Z69667 , AC005202 , Z99754 Genomic DNA. Translation: CAI95590.2 .
Z99754 , AC005202 , Z69667 Genomic DNA. Translation: CAI95600.2 .
Z99754 , AC005202 , Z69667 Genomic DNA. Translation: CAI95601.2 .
BC017447 mRNA. Translation: AAH17447.1 .
BC044648 mRNA. Translation: AAH44648.1 .
CCDSi CCDS10405.1. [O15169-1 ]
CCDS10406.1. [O15169-2 ]
RefSeqi NP_003493.1. NM_003502.3. [O15169-1 ]
NP_851393.1. NM_181050.2. [O15169-2 ]
XP_005255666.1. XM_005255609.2. [O15169-1 ]
UniGenei Hs.592082.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DK8 X-ray 1.57 A 74-220 [» ]
1EMU X-ray 1.90 A 80-211 [» ]
1O9U X-ray 2.40 B 383-400 [» ]
3ZDI X-ray 2.64 B 383-400 [» ]
4B7T X-ray 2.77 B 383-400 [» ]
4NM0 X-ray 2.50 B 383-402 [» ]
4NM3 X-ray 2.10 B 383-402 [» ]
4NM5 X-ray 2.30 B 383-402 [» ]
4NM7 X-ray 2.30 B 383-402 [» ]
4NU1 X-ray 2.50 B 383-402 [» ]
ProteinModelPortali O15169.
SMRi O15169. Positions 74-220, 779-862.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113909. 55 interactions.
DIPi DIP-34630N.
IntActi O15169. 62 interactions.
MINTi MINT-100969.
STRINGi 9606.ENSP00000262320.

Chemistry

ChEMBLi CHEMBL1255127.

PTM databases

PhosphoSitei O15169.

Proteomic databases

MaxQBi O15169.
PaxDbi O15169.
PRIDEi O15169.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262320 ; ENSP00000262320 ; ENSG00000103126 . [O15169-1 ]
ENST00000354866 ; ENSP00000346935 ; ENSG00000103126 . [O15169-2 ]
GeneIDi 8312.
KEGGi hsa:8312.
UCSCi uc002cgp.2. human. [O15169-1 ]
uc002cgq.2. human. [O15169-2 ]

Organism-specific databases

CTDi 8312.
GeneCardsi GC16M000338.
HGNCi HGNC:903. AXIN1.
HPAi CAB012987.
MIMi 114550. phenotype.
603816. gene.
607864. phenotype.
neXtProti NX_O15169.
PharmGKBi PA25195.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG238205.
HOVERGENi HBG004324.
InParanoidi O15169.
KOi K02157.
OMAi IMQWIIE.
OrthoDBi EOG79PJQ0.
PhylomeDBi O15169.
TreeFami TF315454.

Enzyme and pathway databases

Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_200766. degradation of AXIN.
REACT_200777. TCF dependent signaling in response to WNT.
SignaLinki O15169.

Miscellaneous databases

EvolutionaryTracei O15169.
GeneWikii AXIN1.
GenomeRNAii 8312.
NextBioi 31127.
PROi O15169.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15169.
Bgeei O15169.
CleanExi HS_AXIN1.
Genevestigatori O15169.

Family and domain databases

Gene3Di 1.10.196.10. 2 hits.
InterProi IPR014936. Axin_b-cat-bd.
IPR001158. DIX.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF08833. Axin_b-cat_bind. 1 hit.
PF00778. DIX. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view ]
PRINTSi PR01301. RGSPROTEIN.
SMARTi SM00021. DAX. 1 hit.
SM00315. RGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48097. SSF48097. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS50841. DIX. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling pathway that regulates embryonic axis formation."
    Zeng L., Fagotto F., Zhang T., Hsu W., Vasicek T.J., Perry W.L. III, Lee J.J., Tilghman S.M., Gumbiner B.M., Costantini F.
    Cell 90:181-192(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
    Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
    Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 471-862 (ISOFORM 1).
    Tissue: Lymphoma and Renal cell carcinoma.
  5. "Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain."
    Hsu W., Zeng L., Costantini F.
    J. Biol. Chem. 274:3439-3445(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GSK3B AND PPP2CA, PHOSPHORYLATION, DEPHOSPHORYLATION.
  6. "AXIN1 mutations in hepatocellular carcinomas, and growth suppression in cancer cells by virus-mediated transfer of AXIN1."
    Satoh S., Daigo Y., Furukawa Y., Kato T., Miwa N., Nishiwaki T., Kawasoe T., Ishiguro H., Fujita M., Tokino T., Sasaki Y., Imaoka S., Murata M., Shimano T., Yamaoka Y., Nakamura Y.
    Nat. Genet. 24:245-250(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE.
  7. "Low-density lipoprotein receptor-related protein-5 binds to Axin and regulates the canonical Wnt signaling pathway."
    Mao J., Wang J., Liu B., Pan W., Farr G.H. III, Flynn C., Yuan H., Takada S., Kimelman D., Li L., Wu D.
    Mol. Cell 7:801-809(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRP5.
  8. "I-mfa domain proteins interact with Axin and affect its regulation of the Wnt and c-Jun N-terminal kinase signaling pathways."
    Kusano S., Raab-Traub N.
    Mol. Cell. Biol. 22:6393-6405(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MDFI AND MDFIC, FUNCTION.
  9. "Regulation of the Wnt signaling pathway by disabled-2 (Dab2)."
    Howe P.H.
    EMBO J. 22:3084-3094(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2.
  10. "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase activation by Axin and dishevelled through distinct mechanisms."
    Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.
    J. Biol. Chem. 279:39366-39373(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DIXDC1; MAP3K1 AND MAP3K4.
  11. "Increased DNA methylation at the AXIN1 gene in a monozygotic twin from a pair discordant for a caudal duplication anomaly."
    Oates N.A., van Vliet J., Duffy D.L., Kroes H.Y., Martin N.G., Boomsma D.I., Campbell M., Coulthard M.G., Whitelaw E., Chong S.
    Am. J. Hum. Genet. 79:155-162(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CAUDAL DUPLICATION ANOMALY.
  12. "Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia."
    Liu W., Rui H., Wang J., Lin S., He Y., Chen M., Li Q., Ye Z., Zhang S., Chan S.C., Chen Y.-G., Han J., Lin S.-C.
    EMBO J. 25:1646-1658(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMAD6; SMAD7 AND RNF111, FUNCTION, SUBCELLULAR LOCATION.
  13. "Daxx cooperates with the Axin/HIPK2/p53 complex to induce cell death."
    Li Q., Wang X., Wu X., Rui Y., Liu W., Wang J., Wang X., Liou Y.C., Ye Z., Lin S.C.
    Cancer Res. 67:66-74(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAXX, IDENTIFICATION AS A COMPONENT OF THE AXIN1-HIPK2-TP53 COMPLEX, SUBCELLULAR LOCATION, FUNCTION.
  14. "Protein phosphatase 1 regulates assembly and function of the beta-catenin degradation complex."
    Luo W., Peterson A., Garcia B.A., Coombs G., Kofahl B., Heinrich R., Shabanowitz J., Hunt D.F., Yost H.J., Virshup D.M.
    EMBO J. 26:1511-1521(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-75; SER-77; SER-217 AND SER-469, INTERACTION WITH GSK3B AND PPP1CA, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "SUMOylation target sites at the C terminus protect Axin from ubiquitination and confer protein stability."
    Kim M.J., Chia I.V., Costantini F.
    FASEB J. 22:3785-3794(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: ADP-RIBOSYLATION, UBIQUITINATION, DOMAIN TANKYRASE-BINDING MOTIF, INTERACTION WITH TNKS AND TNKS2.
  18. "The Ubiquitin specific protease USP34 regulates Axin stability and Wnt/beta-catenin signaling."
    Lui T.T., Lacroix C., Ahmed S.M., Goldenberg S.J., Leach C.A., Daulat A.M., Angers S.
    Mol. Cell. Biol. 31:2053-2065(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP34, SUBCELLULAR LOCATION.
  19. "RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling."
    Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A., Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M., Porter J.A., Huang S.M., Cong F.
    Nat. Cell Biol. 13:623-629(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION, UBIQUITINATION, INTERACTION WITH RNF146; TNKS AND TNKS2.
  20. Cited for: INTERACTION WITH TNKS, UBIQUITINATION.
  21. "Structural basis of the axin-adenomatous polyposis coli interaction."
    Spink K.E., Polakis P., Weis W.I.
    EMBO J. 19:2270-2279(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 74-220 IN COMPLEX WITH APC.
  22. "Structural basis for recruitment of glycogen synthase kinase 3beta to the axin-APC scaffold complex."
    Dajani R., Fraser E., Roe S.M., Yeo M., Good V.M., Thompson V., Dale T.C., Pearl L.H.
    EMBO J. 22:494-501(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 383-400 IN COMPLEX WITH GSK3B.
  23. "Mutational spectrum of beta-catenin, AXIN1, and AXIN2 in hepatocellular carcinomas and hepatoblastomas."
    Taniguchi K., Roberts L.R., Aderca I.N., Dong X., Qian C., Murphy L.M., Nagorney D.M., Burgart L.J., Roche P.C., Smith D.I., Ross J.A., Liu W.
    Oncogene 21:4863-4871(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HCC ARG-106; LEU-345; SER-425 AND SER-650, VARIANT HEPATOBLASTOMA GLN-841.

Entry informationi

Entry nameiAXIN1_HUMAN
AccessioniPrimary (citable) accession number: O15169
Secondary accession number(s): Q4TT26
, Q4TT27, Q86YA7, Q8WVW6, Q96S28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 10, 2002
Last modified: September 3, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi